CHARACTERIZATION OF A CARTILAGE-DERIVED 66-KDA PROTEIN (RGD-CAP BETA-IG-H3) THAT BINDS TO COLLAGEN/

Citation
K. Hashimoto et al., CHARACTERIZATION OF A CARTILAGE-DERIVED 66-KDA PROTEIN (RGD-CAP BETA-IG-H3) THAT BINDS TO COLLAGEN/, Biochimica et biophysica acta. Molecular cell research, 1355(3), 1997, pp. 303-314
Citations number
39
Categorie Soggetti
Biology,Biophysics
ISSN journal
01674889
Volume
1355
Issue
3
Year of publication
1997
Pages
303 - 314
Database
ISI
SICI code
0167-4889(1997)1355:3<303:COAC6P>2.0.ZU;2-B
Abstract
A 66-kDa collagen fiber-associated protein (RGD-CAP) was isolated from a fiber-rich fraction of pig cartilage by ultrafiltration and collage n-affinity chromatography. Amino acid sequencing and cDNA cloning indi cated that the RGD-CAP is identical or closely related to beta ig-h3 p rotein which is induced in human adenocarcinoma cells by transforming growth factor-beta (TGF-beta) (Skonier, J., Neubauer, M., Madisen, L., Bennett, K., Plowman, G.D., and Purchio, A.F. (1992) DNA Cell. Biol. 11, 511-522). The RGD-CAP, as well as beta ig-h3, has the RGD sequence in the C-terminal region. The native RGD-CAP bound to type I, II, and IV collagens even in the presence of 1 M NaCl. A recombinant preparat ion of RGD-CAP expressed in Escherichia coli cells also bound to colla gen but not to gelatin. The RGD-CAP mRNA was expressed in chondrocytes throughout all stages, although the expression level was highest duri ng the prehypertrophic stage. In addition, TGF-beta increased the RGD- CAP mRNA level in chondrocyte cultures. Since RGD-CAP transcripts were found in most tissues, this novel collagen-binding protein may play a n important role in cell-collagen interactions in various tissues incl uding developing cartilage.